Download MendeleyCrystal structure of Rossmann-fold protein of unknown function (DUF574) (NP_823353.1) from Streptomyces avermitilis MA-4680 at 1.80 A resolution
Joint Center for Structural Genomics (JCSG)To be published.
3GO4
Crystal structure of a duf574 family protein (sav_2177) from streptomyces avermitilis ma-4680 at 1.80 A resolution
- PDB DOI: https://doi.org/10.2210/pdb3GO4/pdb
- Classification: UNKNOWN FUNCTION
- Organism(s): Streptomyces avermitilis MA-4680 = NBRC 14893
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2009-03-18 Released: 2009-04-14
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.250
- R-Value Work: 0.200
- R-Value Observed: 0.202
Starting Model: experimental
View more details
This is version 1.7 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Protein of unknown function DUF574 | 277 | Streptomyces avermitilis MA-4680 = NBRC 14893 | Mutation(s): 0 Gene Names: NP_823353.1, SAV2177, SAV_2177 |  | |
UniProt | |||||
Find proteins for Q82L35 (Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)) Explore Q82L35 Go to UniProtKB: Q82L35 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q82L35 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| SAH Query on SAH | B [auth A] | S-ADENOSYL-L-HOMOCYSTEINE C14 H20 N6 O5 S ZJUKTBDSGOFHSH-WFMPWKQPSA-N |  | ||
| SO4 Query on SO4 | C [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| EDO Query on EDO | D [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.250
- R-Value Work: 0.200
- R-Value Observed: 0.202
- Space Group: C 1 2 1
- Diffraction Data: https://doi.org/10.18430/M33GO4
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 94.637 | α = 90 |
| b = 49.439 | β = 123.8 |
| c = 77.811 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| PHENIX | refinement |
| MolProbity | model building |
| XSCALE | data scaling |
| PDB_EXTRACT | data extraction |
| MAR345 | data collection |
| XDS | data reduction |
| MOLREP | phasing |
Entry History
Deposition Data
- Released Date: 2009-04-14 Deposition Author(s): Joint Center for Structural Genomics (JCSG)
Revision History (Full details and data files)
- Version 1.0: 2009-04-14
Type: Initial release - Version 1.1: 2011-07-13
Changes: Source and taxonomy, Version format compliance - Version 1.2: 2017-11-01
Changes: Refinement description - Version 1.3: 2019-07-24
Changes: Data collection, Derived calculations, Refinement description - Version 1.4: 2023-02-01
Changes: Database references, Derived calculations - Version 1.5: 2023-09-20
Changes: Data collection, Refinement description - Version 1.6: 2023-11-22
Changes: Data collection - Version 1.7: 2024-11-06
Changes: Data collection, Structure summary
